-
Correlation of exons with structural domains in alcohol dehydrogenase.
The intron/exon arrangement in the gene sequence of maize alcohol dehydrogenase has been compared to the three dimensional structure of liver alcohol dehydrogenase. The co-enzyme binding domain is separated from the catalytic domain by introns four and nine. Intron seven separates the co-enzyme binding domain into two structurally similar mononucleotide binding units. The first of these units is divided by introns five and six into three structurally similar alpha beta modules. Implications of these results for protein evolution is discussed. All splice junctions map close to or at the surface of the domains, and several of these cannot be identified by distance maps.
PMID: 6378620 [PubMed - indexed for MEDLINE]
PMCID: PMC557513
-
Cited by 17 PubMed Central articles
-
Pea formaldehyde-active class III alcohol dehydrogenase: common derivation of the plant and animal forms but not of the corresponding ethanol-active forms (classes I and P).
Shafqat J, El-Ahmad M, Danielsson O, Martínez MC, Persson B, Parés X, Jornvall H.
Proc Natl Acad Sci U S A. 1996 May 28; 93(11):5595-9.
[Proc Natl Acad Sci U S A. 1996]
-
Molecular evolution of the Adh1 locus in the genus Zea.
Gaut BS, Clegg MT.
Proc Natl Acad Sci U S A. 1993 Jun 1; 90(11):5095-9.
[Proc Natl Acad Sci U S A. 1993]
-
Phosphoglucomutase 1: a gene with two promoters and a duplicated first exon.
Putt W, Ives JH, Hollyoake M, Hopkinson DA, Whitehouse DB, Edwards YH.
Biochem J. 1993 Dec 1; 296 ( Pt 2):417-22.
[Biochem J. 1993]
- » See all...